Theoretical studies of strong attractive interaction between macro-anions mediated by multivalent metal cations and related association behavior: Effective interaction between ATP-binding proteins can be regulated by hydrolysis

研究成果: 著書/レポートタイプへの貢献

抄録

In this chapter, calculated effective interactions between macro-anions are introduced. The macro-anions are effectively attracted to each other under certain conditions, and the aggregation behavior of macro-anions is discussed on the basis of the calculated effective interactions. The success of models that simulate the behavior of such systems indicates that theoretical discussions are important to understanding the observed aggregation of acidic proteins in solution of multivalent cations. The hydrolysis of ATP regulates the effective interaction between ATP-binding proteins, such as actin monomers. The regulation of effective interaction is discussed from the viewpoint of the calculated effective interaction between macro-anions.

元の言語英語
ホスト出版物のタイトルThe Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery
出版者Springer Singapore
ページ53-67
ページ数15
ISBN(電子版)9789811084591
ISBN(印刷物)9789811084584
DOI
出版物ステータス出版済み - 5 7 2018

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Anions
Macros
Cations
Hydrolysis
Carrier Proteins
Theoretical Models
Adenosine Triphosphate
Metals
Association reactions
Agglomeration
Actins
Monomers
Proteins

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)

これを引用

Theoretical studies of strong attractive interaction between macro-anions mediated by multivalent metal cations and related association behavior : Effective interaction between ATP-binding proteins can be regulated by hydrolysis. / Akiyama, Ryo.

The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Springer Singapore, 2018. p. 53-67.

研究成果: 著書/レポートタイプへの貢献

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